1lwd
From Proteopedia
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CRYSTAL STRUCTURE OF NADP-DEPENDENT ISOCITRATE DEHYDROGENASE FROM PORCINE HEART MITOCHONDRIA
Overview
The crystal structure of porcine heart mitochondrial NADP+-dependent, isocitrate dehydrogenase (IDH) complexed with Mn2+ and isocitrate was, solved to a resolution of 1.85 A. The enzyme was expressed in Escherichia, coli, purified as a fusion protein with maltose binding protein, and, cleaved with thrombin to yield homogeneous enzyme. The structure was, determined by multiwavelength anomalous diffraction phasing using selenium, substitution in the form of selenomethionine as the anomalous scatterer., The porcine NADP+-IDH enzyme is structurally compared with the previously, solved structures of IDH from E. coli and Bacillus subtilis that share 16, and 17% identity, respectively, with the mammalian enzyme. The porcine, enzyme has a protein fold similar to the bacterial IDH structures with, ... [(full description)]
About this Structure
1LWD is a [Single protein] structure of sequence from [Sus scrofa] with MN, SO4 and ICT as [ligands]. Active as [Isocitrate dehydrogenase (NADP(+))], with EC number [1.1.1.42]. Structure known Active Sites: MN1 and MN2. Full crystallographic information is available from [OCA].
Reference
Crystal structure of porcine mitochondrial NADP+-dependent isocitrate dehydrogenase complexed with Mn2+ and isocitrate. Insights into the enzyme mechanism., Ceccarelli C, Grodsky NB, Ariyaratne N, Colman RF, Bahnson BJ, J Biol Chem. 2002 Nov 8;277(45):43454-62. Epub 2002 Aug 30. PMID:12207025
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